The invariant arginine in motif 2 of Escherichia coli alanyl-tRNA synthetase is important for catalysis but not for substrate binding.

Y. Lu; K.A. Hill

doi:10.1016/s0021-9258(17)32691-1

The invariant arginine in motif 2 of Escherichia coli alanyl-tRNA synthetase is important for catalysis but not for substrate binding.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)32691-1 ◽

1994 ◽

Vol 269 (16) ◽

pp. 12137-12141 ◽

Cited By ~ 1

Author(s):

Y. Lu ◽

K.A. Hill

Keyword(s):

Escherichia Coli ◽

Substrate Binding ◽

Trna Synthetase

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Order of substrate binding to tyrosyl-tRNA synthetase of Escherichia coli B

FEBS Letters ◽

10.1016/0014-5793(71)80224-7 ◽

1971 ◽

Vol 13 (3) ◽

pp. 157-160 ◽

Cited By ~ 26

Author(s):

Daniel V. Santi ◽

Van A. Peña

Keyword(s):

Escherichia Coli ◽

Substrate Binding ◽

Trna Synthetase ◽

Escherichia Coli B

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Contributions of the substrate-binding arginine residues to maleate-induced closure of the active site of Escherichia coli aspartate aminotransferase

European Journal of Biochemistry ◽

10.1046/j.1432-1033.2001.02035.x ◽

2001 ◽

Vol 268 (6) ◽

pp. 1640-1645

Author(s):

Annelise Matharu ◽

Hideyuki Hayashi ◽

Hiroyuki Kagamiyama ◽

Bruno Maras ◽

Robert A. John

Keyword(s):

Escherichia Coli ◽

Active Site ◽

Aspartate Aminotransferase ◽

Substrate Binding ◽

Arginine Residues

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Faculty Opinions recommendation of A conserved threonine within Escherichia coli leucyl-tRNA synthetase prevents hydrolytic editing of leucyl-tRNALeu.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1000366.1351 ◽

2001 ◽

Author(s):

Anne-Catherine Dock-Bregeon

Keyword(s):

Escherichia Coli ◽

Trna Synthetase

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Faculty Opinions recommendation of Discrimination of tRNA(Leu) isoacceptors by the mutants of Escherichia coli leucyl-tRNA synthetase in editing.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1009103.118807 ◽

2002 ◽

Author(s):

Anne-Catherine Dock-Bregeon

Keyword(s):

Escherichia Coli ◽

Trna Synthetase

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Faculty Opinions recommendation of Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1020064.228494 ◽

2004 ◽

Author(s):

Eric Miller

Keyword(s):

Escherichia Coli ◽

Substrate Binding ◽

Binding Properties ◽

Protein Deacetylase

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The catalytic mechanism of the glutamyl-tRNA synthetase from Escherichia coli. Detection of an intermediate complex in which glutamate is activated.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)85976-8 ◽

1980 ◽

Vol 255 (5) ◽

pp. 1956-1961

Author(s):

D. Kern ◽

J. Lapointe

Keyword(s):

Escherichia Coli ◽

Catalytic Mechanism ◽

Trna Synthetase ◽

Intermediate Complex

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Purification and properties of alanine tRNA synthetase from Escherichia coli A tetramer of identical subunits.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)70119-7 ◽

1981 ◽

Vol 256 (1) ◽

pp. 198-204 ◽

Cited By ~ 2

Author(s):

S.D. Putney ◽

R.T. Sauer ◽

P.R. Schimmel

Keyword(s):

Escherichia Coli ◽

Trna Synthetase ◽

Purification And Properties

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31P NMR of the reversible methionine activation reaction catalyzed by methionyl-tRNA synthetase of Escherichia coli. Equilibrium, interconversion rates, and NMR parameters of the enzyme-bound species.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)70624-3 ◽

1980 ◽

Vol 255 (17) ◽

pp. 8164-8169

Author(s):

G. Fayat ◽

S. Blanquet ◽

B.D. Nageswara Rao ◽

M. Cohn

Keyword(s):

Escherichia Coli ◽

31P Nmr ◽

Trna Synthetase ◽

Activation Reaction ◽

Nmr Parameters ◽

Methionyl Trna Synthetase

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Nucleotide and deduced amino acid sequence of human threonyl-tRNA synthetase reveals extensive homology to the Escherichia coli and yeast enzymes

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)92906-6 ◽

1991 ◽

Vol 266 (15) ◽

pp. 9919-9923

Author(s):

M.E. Cruzen ◽

S.M. Arfin

Keyword(s):

Escherichia Coli ◽

Amino Acid ◽

Amino Acid Sequence ◽

Trna Synthetase

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Covalent modification of substrate-binding sites of Escherichia coli ADP-glucose synthetase. Isolation and structural characterization of 8-azido-ADP-glucose-incorporated peptides.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)36052-0 ◽

1986 ◽

Vol 261 (3) ◽

pp. 1058-1064

Author(s):

Y M Lee ◽

J Preiss

Keyword(s):

Escherichia Coli ◽

Structural Characterization ◽

Binding Sites ◽

Substrate Binding ◽

Covalent Modification ◽

Substrate Binding Sites

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